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Database: UniProt
Entry: V5IHX3_IXORI
LinkDB: V5IHX3_IXORI
Original site: V5IHX3_IXORI 
ID   V5IHX3_IXORI            Unreviewed;       813 AA.
AC   V5IHX3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative low-density lipoprotein receptor {ECO:0000313|EMBL:JAB80281.1};
DE   Flags: Fragment;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB80281.1};
RN   [1] {ECO:0000313|EMBL:JAB80281.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB80281.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; GANP01004187; JAB80281.1; -; mRNA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 6.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00057; Ldl_recept_a; 7.
DR   Pfam; PF00058; Ldl_recept_b; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 7.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 7.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 7.
DR   PROSITE; PS51120; LDLRB; 4.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:JAB80281.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:JAB80281.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        735..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          309..324
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01186"
FT   REPEAT          412..455
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          456..498
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          499..542
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          543..585
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          792..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        4..16
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        11..29
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        45..57
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        52..70
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        85..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        92..110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        104..119
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        124..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        131..149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        143..158
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        187..202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        206..218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        213..231
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        225..240
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        255..273
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB80281.1"
SQ   SEQUENCE   813 AA;  90759 MW;  C0A0D4032C0F7D23 CRC64;
     KRTCSQTEFR CKNGNCIPSR WQCDNENDCE DKSDEDVVTC SNKTCSEEQF TCKSQECIPI
     TWRCDGQEDC VDGSDEKDEC LAATCTHEEF SCNNGKCITK RWVCDQDDDC GDGSDEKGCA
     NVTCSSAEFM CSNGRCIPDR WHCDGDIDCL DGSDERNCPT TGRPSPCKVR EFQCANGVDC
     IHTSWQCDGD PDCPDESDEA NCTNTCRPDQ FQCRNLHCIP GLLECNGKVE CPDRSDEDHC
     NTTVNRCNPD SEFDCGGNHC IPKHLVCDGK NDCGAFEDEP RELCHKNECS SGHSGCSDIC
     KDDPIGFHCE CHPGFKLTED NRTCDDVDEC LIPGSCSQKC TNYKGGYKCE CIEGYVPEPR
     DRHRCKAKEG VPFLLFANRN DIRKINLETG EYVEVVSKLR STIAMDYIYQ TGTVIWSDTV
     KEEISSAPID TGAPTKVIIN EDLHVADGLA VDWIYNHVYW TDTAQNLISV ADLDGKNRKA
     LFSEDLDEPR AIVVNPLEGW MFWTDWGKQP KIERSGMDGS HRSAIVTTDI LWPNGLAIDF
     VSKQLFWVDA KLHLIGSSDY NGNNRRVILS SPILVKHPFS LDVFEDWLYW TDWESEVINK
     VNKFTGANLE PVLANGVYSP MDIHVYHSYK TRPQRRRTNC KPANGQCSHL CLPAPSISPH
     SAKFSCACPN KMELQEDGHN CRIVETLVST TLRPSTVAAV TDETVVYNAS HNEVSAQPSV
     GHEGLAGKAX XXGKLAGIVI GVLGGLAIIF TLIGYVVYRQ CLRRNITSMN FDNPVYRKTT
     EDQFSLEKNQ YQPARSYPPS MEPLTSPGTN EFV
//
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